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Published 9 December 2002. doi:10.1083/jcb.200205068
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© The Rockefeller University Press, 0021-9525/2002/12/807 $5.00
The Journal of Cell Biology, Volume 159, Number 5, 807-819

Article

 The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint

Tatiana Iouk1, Oliver Kerscher2, Robert J. Scott1, Munira A. Basrai2 and Richard W. Wozniak1

1 Department of Cell Biology, University of Alberta, Edmonton, Alberta, T6G 2H7 Canada
2 Genetics Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20889

Address correspondence to Richard W. Wozniak, Dept. of Cell Biology, University of Alberta, 5-14 Medical Sciences Building, Edmonton, Alberta, T6G 2H7 Canada. Tel.: (780) 492-1384. Fax: (780) 492-0450. E-mail: rick.wozniak{at}ualberta.ca; or Munira A. Basrai, Genetics Branch, Center for Cancer Research, National Cancer Institute, 8901 Wisconsin Ave., NNML Bldg. 8, Rm. 5101, National Institutes of Health, Bethesda, MD 20889-5101. Tel.: (301) 402-2552. Fax: (301) 480-0380. E-mail: basraim{at}nih.gov

Aphysical and functional link between the nuclear pore complex (NPC) and the spindle checkpoint machinery has been established in the yeast Saccharomyces cerevisiae. We show that two proteins required for the execution of the spindle checkpoint, Mad1p and Mad2p, reside predominantly at the NPC throughout the cell cycle. There they are associated with a subcomplex of nucleoporins containing Nup53p, Nup170p, and Nup157p. The association of the Mad1p–Mad2p complex with the NPC requires Mad1p and is mediated in part by Nup53p. On activation of the spindle checkpoint, we detect changes in the interactions between these proteins, including the release of Mad2p (but not Mad1p) from the NPC and the accumulation of Mad2p at kinetochores. Accompanying these events is the Nup53p-dependent hyperphosphorylation of Mad1p. On the basis of these results and genetic analysis of double mutants, we propose a model in which Mad1p bound to a Nup53p-containing complex sequesters Mad2p at the NPC until its release by activation of the spindle checkpoint. Furthermore, we show that the association of Mad1p with the NPC is not passive and that it plays a role in nuclear transport.

Key Words: nucleoporins; cell cycle; kinetochore; mads; nuclear transport


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